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Related Experiment Videos

Phosphorylation of complement factor C3 in vivo.

S C Martin1

  • 1Department of Medical and Physiological Chemistry, Uppsala University, Sweden.

The Biochemical Journal
|August 1, 1989
PubMed
Summary
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Complement factor C3 and S protein (vitronectin) are phosphorylated in blood. Purified C3 is a phosphoprotein in vivo, indicating a role for phosphorylation in complement system regulation.

Area of Science:

  • Biochemistry
  • Immunology
  • Proteomics

Background:

  • The complement system is crucial for innate immunity.
  • Complement factor C3 is central to complement activation.
  • Phosphorylation is a key post-translational modification regulating protein function.

Purpose of the Study:

  • To investigate the phosphorylation status of complement factor C3 and S protein (vitronectin) in various blood conditions.
  • To determine if purified C3 is a phosphoprotein in vivo.
  • To measure ATP concentration in plasma.

Main Methods:

  • Analysis of phosphorylated proteins in EDTA- and heparin-anticoagulated whole blood.
  • Investigation of protein phosphorylation in coagulating blood.
  • Biochemical analysis of purified C3.

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  • Measurement of plasma ATP concentration.

    • Main Results:

    • Complement factor C3 and S protein (vitronectin) were found to be phosphorylated in whole blood and coagulating blood.
    • Purified C3 was confirmed as a phosphoprotein in vivo, containing 0.15 mol of alkali-labile phosphate/mol of protein.
    • Plasma ATP concentration was measured at approximately 2 microM.

    Conclusions:

    • Complement factor C3 and S protein (vitronectin) undergo phosphorylation in blood.
    • C3 functions as a phosphoprotein in vivo, suggesting phosphorylation influences its biological activity.
    • The presence of ATP in plasma supports the potential for C3 phosphorylation in vivo.